What question did this study set out to answer?

To determine the receptor capabilities of integrin VLA-3 for collagen, laminin, and fibronectin, and characterize the regulatory roles of RGD peptides and divalent cations.

January 1, 1991The Journal of Cell BiologyOpen Access

Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations.

View Full Paper

Ask AI

Bookmark

Authors

MEMariano J. ElicesUniversidad San Pablo CEU LULisa A. UrryTufts University MHMartin E. HemlerBoston University

Discussion

Member takes

Implication

In vitro study demonstrates distinct RGD dependency and cation sensitivity for VLA-3 binding in lung carcinoma cells, indicating multi-modal matrix recognition.

Key Points

To determine the receptor capabilities of integrin VLA-3 for collagen, laminin, and fibronectin, and characterize the regulatory roles of RGD peptides and divalent cations.
Assayed whole cell adhesion using the NCI-H69 small cell lung carcinoma cell line, which expresses VLA-3 with minimal expression of other integrins.
Evaluated ligand binding mechanisms via ligand affinity chromatography columns, competitive inhibition with Arg-Gly-Asp (RGD) peptide, and exposure to Ca++, Mg++, and Mn++ cations.
VLA-3 mediated adhesion to fibronectin in an RGD-dependent manner, whereas VLA-3-mediated binding to collagen and laminin was not inhibited by RGD peptide and was unaffected by VLA-5.
VLA-3-mediated binding to fibronectin increased 6.6-fold in the presence of Mg++ and 30-fold with Mn++ compared to Ca++, whereas binding to collagen increased only 1.2-fold with Mg++ and 1.7-fold with Mn++.

Cite This Study

Elices et al. (1991) studied this question.

synapsesocial.com/papers/6a6f4a006c240de38cdb6f72 https://doi.org/10.1083/jcb.112.1.169

View Full Paper

Ask AI

Bookmark

January 1, 1991The Journal of Cell BiologyOpen Access

Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations.

View Full Paper

Ask AI

Bookmark

Authors

MEMariano J. ElicesUniversidad San Pablo CEU LULisa A. UrryTufts University MHMartin E. HemlerBoston University

Discussion

Member takes

Implication

In vitro study demonstrates distinct RGD dependency and cation sensitivity for VLA-3 binding in lung carcinoma cells, indicating multi-modal matrix recognition.

Key Points

To determine the receptor capabilities of integrin VLA-3 for collagen, laminin, and fibronectin, and characterize the regulatory roles of RGD peptides and divalent cations.
Assayed whole cell adhesion using the NCI-H69 small cell lung carcinoma cell line, which expresses VLA-3 with minimal expression of other integrins.
Evaluated ligand binding mechanisms via ligand affinity chromatography columns, competitive inhibition with Arg-Gly-Asp (RGD) peptide, and exposure to Ca++, Mg++, and Mn++ cations.
VLA-3 mediated adhesion to fibronectin in an RGD-dependent manner, whereas VLA-3-mediated binding to collagen and laminin was not inhibited by RGD peptide and was unaffected by VLA-5.
VLA-3-mediated binding to fibronectin increased 6.6-fold in the presence of Mg++ and 30-fold with Mn++ compared to Ca++, whereas binding to collagen increased only 1.2-fold with Mg++ and 1.7-fold with Mn++.

Cite This Study

Elices et al. (1991) studied this question.

synapsesocial.com/papers/6a6f4a006c240de38cdb6f72 https://doi.org/10.1083/jcb.112.1.169

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark